ID M3IME9_CANMX Unreviewed; 1061 AA.
AC M3IME9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=ATP-dependent RNA helicase DOB1 {ECO:0000313|EMBL:EMG47551.1};
GN ORFNames=G210_2054 {ECO:0000313|EMBL:EMG47551.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47551.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47551.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000256|ARBA:ARBA00010140}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG47551.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOGT01001493; EMG47551.1; -; Genomic_DNA.
DR AlphaFoldDB; M3IME9; -.
DR STRING; 1245528.M3IME9; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_0_1_1; -.
DR OMA; IMLKNYN; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF7; EXOSOME RNA HELICASE MTR4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EMG47551.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT DOMAIN 150..306
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 386..587
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 120489 MW; 0BD41B233615D599 CRC64;
MDDLFDVFDE APQQAPPKIE ELKQEEEHSP SVVTNNKKRP NDQQLEPKKT SSSSSKKVKQ
HEDIKPVVFD SVEIEASIEV KASDGLMAPS TTSTTTNTTG EGDKLKLRHQ VRHQVAVPPS
YPYTPIGEHK REKDARTYPF TLDPFQDTAI SCIDRNESVL VSAHTSAGKT VVAEYAIAQS
LRDKQRVIYT SPIKALSNQK YRELQAIFGD VGLMTGDVTI NPDAGCLVMT TEILRSMLYR
GSEVMREVAW VVFDEVHYMR DKSRGVVWEE TIILLPDKVH YVFLSATIPN AMEFAEWIVK
IHNQPCHVVY TDFRPTPLQH YLFPAGGDGI HLVVDEKGTF REENFQKAMT TIGDNTGDDP
NADNSRGKKG KTFKGGNKDG KSDIYKIVKM IYMKKYNPVI VFSFSKRECE SLALKMSKLD
FNTDEERQAL TQIFNNAIEL LPENDRDLPQ IKNILPLLKR GIGIHHSGLL PILKEIIEIL
FQEGFLKVLF ATETFSIGLN MPAKTVVFTS VRKWDGVGFR WVSGGEYIQM SGRAGRRGLD
DRGIVIMMID EKMEPQVAKG MVKGQADRLD SAFHLGYNMI LNLMRVEGIS PEYMLENSFF
QFQKAASVPV MEQKLITCKE EIEDIHIEDE PIIKEYYDLQ QQLNKYAEDV RKVITHPGNS
LPFLQDGRVI KVKIGQQDYG WGMVTTFTKR NRRSQQEEFL PHEAYVVEVF VTTMYVDSPV
NLIKKFNPLL PEGIRPGKPG EQTRAEFISI TLDSIEKIST VRLRVPDDHK SSAAKRTLVK
TLQDLPKRLP DGIPLIDPVT SMKITDDDFK KLLHKIDILE SKLSSNPLHN SARLDDLYKK
YSHKMTLENQ VKQLKEKIFQ AEAVVQLDEL SNIKRVLKKL EFTGPNEIVE LKGRVAAEIS
TGDELMITEL LFSGFFNDLT PQQICGLLSS FIFQERAKEL PKLKPDLAEP AKIIQETASK
IAKISRQCNL EIIEKDYVES FNLALIEVVF AWSNNASFSS ICKMTDIYEG AIIRAIRREI
ELIKQLVDAA KIIGNQELVD KFEKCIELLN RDFVQVSSLY M
//